- FASTA Sequence
- mmCIF Format
- mmCIF Format (Header)
- Legacy PDB Format
- Legacy PDB Format (Header)
- More on PDB File Formats
Cryo-EM structure of human insulin receptor bound to 4 IGF-I, conformation 3
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A | SCOP2B Superfamily | L domain-like | 8032832 | 3001010 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | Growth factor receptor domain-like | 8032837 | 3000398 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | L domain-like | 8032830 | 3001010 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | L domain-like | 8032832 | 3001010 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | L domain-like | 8032830 | 3001010 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | Growth factor receptor domain-like | 8032837 | 3000398 | SCOP2B (2022-06-29) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source | |
---|---|---|---|---|---|---|
PF00757 | Furin-like cysteine rich region (Furin-like) | Furin-like cysteine rich region | Domain | |||
PF00041 | Fibronectin type III domain (fn3) | Fibronectin type III domain | Domain | |||
PF01030 | Receptor L domain (Recep_L_domain) | Receptor L domain | - | Repeat | ||
PF17870 | Insulin receptor trans-membrane segment (Insulin_TMD) | Insulin receptor trans-membrane segment | This entry represents the trans-membrane domain (TMD) found in insulin receptor proteins. The TMD of the insulin receptor is within the beta-subunit and contains 23 amino acids. Mutations in the TMD were shown to have effects on receptor biosynthetic ... | This entry represents the trans-membrane domain (TMD) found in insulin receptor proteins. The TMD of the insulin receptor is within the beta-subunit and contains 23 amino acids. Mutations in the TMD were shown to have effects on receptor biosynthetic processing and kinase activation. Substitution of the entire TMD of the insulin receptor (IR) resulted in constitutive kinase activation in vitro, while replacing the TMD with that of glycophorin A inhibited insulin action. Structural studies show that TMD contains a helix and a kink when it is purified in dodecylphosphocholine (DPC) micelles. The residues 942-948 preceding the TMD have a propensity to be a short helix and may interact with membrane [1]. | Domain | |